EC Number   |
General Information |
Reference |
|---|
   1.14.18.3 | evolution |
methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available |
-, 745389 |
| 1.14.18.3 | evolution |
the enzyme is a member of the copper-containing membrane monooxygenase (CuMMO) superfamily |
-, 745721 |
| 1.14.18.3 | malfunction |
inactivation of the particulate methane monooxygenase (pMMO): the enzyme oxidizes acetylene to the ketene (C2H2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit. LC-MS/MS analysis of the peptides derived from in-gel proteolytic digestion of the protein subunit identifies K196 of PmoC as the site of acetylation. No evidence is obtained for chemical modification of the PmoA or PmoB subunit. The inactivation of pMMO by a single adduct in the transmembrane PmoC domain is intriguing given the complexity of the structural fold of this large membrane-protein complex as well as the complicated roles played by the various metal cofactors in the enzyme catalysis. Computational studies suggest that the entry of hydrophobic substrates to, and migration of products from, the catalytic site of pMMO are controlled tightly within the transmembrane domain |
-, 744405 |
| 1.14.18.3 | metabolism |
ammonia-supplied Methylosinus trichosporium OB3b containing soluble methane monooxygenase (sMMO) grow at the fastest rate, while the highest poly-beta-hydroxybutyrate content is obtained by transferring nitrate-supplied bacteria with the expression of particulate methane monooxygenase (pMMO) to nitrogen-free mineral salts (NFMS) + 0.005 mmol/l Cu medium. The slightly lower growth rate and lower cell yield of ammonia supplied bacteria expressing particulate methane monooxygenase (pMMO) might be attributed to high similarity between the gene encoding particulate methane monooxygenase (pMMO) and the sequence of the ammoniamonooxygenase gene. The methane monooxygenase activity, growth rate and intracellular poly-beta-hydroxybutyrate content of bacteria expressing pMMO are greatly decreased after being continuously cultivated with N2. However, in the cyclic NO3-N2 cultivation regime, the activity of N2-fixing bacteria expressing pMMO is significantly increased |
745453 |
| 1.14.18.3 | metabolism |
during production of particulate methane monooxygenase, the majority of quinones are directed to methane oxidation |
-, 745730 |
| 1.14.18.3 | metabolism |
in the initial steps of their metabolic pathway, methanotrophic bacteria oxidize methane to methanol with methane monooxygenases (MMOs) and methanol to formaldehyde with methanol dehydrogenases (MDHs). Membrane-bound particulate MMO (pMMO) and MDH interact to form a metabolic supercomplex, interaction analysis and biolayer interferometry studies demonstrate specific protein-protein interactions between methanol dehydrogenase (MDH) and Methyylococcus capsulatus (Bath) pMMO as well as between MDH and the truncated recombinant periplasmic domains of pMMO (spmoB), kinetics, overview |
-, 744325 |
| 1.14.18.3 | metabolism |
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, analysis of the mechanism of the copper switch. Transcriptomic profiling of particulate MMO and soluble MMO, EC 1.14.13.25, using Methylococcus capsulatus DNA microarrays. 137 ORFs are found to be differentially expressed between cells producing sMMO and pMMO, while only minor differences in gene expression are observed between the pMMO-producing cultures. Of these, 87 genes are upregulated during sMMO-producing cells, i.e. during copper-limited growth. Major changes takes place in the respiratory chain between pMMO-and sMMO-producing cells, and quinone are predominantly used as the electron donors for methane oxidation by pMMO. Proposed pathway of methane oxidation in Methylococcus capsulatus cells producing either sMMO or pMMO, overview |
-, 745730 |
| 1.14.18.3 | more |
analysis of structural and functional differences of sMMO, EC 1.14.13.25, and pMMO, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview |
-, 746420 |
| 1.14.18.3 | more |
enzyme pMMO contains a copper active site, active site structure, overview |
745389 |
| 1.14.18.3 | more |
enzyme pMMO contains a copper active site, active site structure, overview. Density functional theory and quantum mechanics/molecular mechanics calculations using the Methylococcus capsulatus pMMO structure as a starting model suggesting that a mononuclear copper active site may be viable, proceeding through a CuIII-oxo (CuII-O·) species |
-, 745389 |
